메뉴 건너뛰기




Volumn 11, Issue 1, 2016, Pages

Novel α-L-fucosidases from a soil metagenome for production of fucosylated human milk oligosaccharides

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA LEVO FUCOSIDASE; OLIGOSACCHARIDE; FUCOSE;

EID: 84958191367     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0147438     Document Type: Article
Times cited : (66)

References (38)
  • 1
    • 0033031589 scopus 로고    scopus 로고
    • L-Fucose: Occurrence, physiological role, chemical, enzymatic and microbial synthesis
    • Vanhooren PT, Vandamme EJ. L-Fucose: Occurrence, physiological role, chemical, enzymatic and microbial synthesis. J Chem Technol Biot. 1999; 74: 479-497.
    • (1999) J Chem Technol Biot. , vol.74 , pp. 479-497
    • Vanhooren, P.T.1    Vandamme, E.J.2
  • 2
    • 0038495798 scopus 로고    scopus 로고
    • Fucose: Biosynthesis and biological function in mammals
    • 12651883
    • Becker DJ, Lowe JB. Fucose: Biosynthesis and biological function in mammals. Glycobiology. 2003; 13: 41R-53R. PMID: 12651883
    • (2003) Glycobiology. , vol.13 , pp. 41R-53R
    • Becker, D.J.1    Lowe, J.B.2
  • 3
    • 84864465909 scopus 로고    scopus 로고
    • Human milk oligosaccharides: Every baby needs a sugar mama
    • 22513036
    • Bode L. Human milk oligosaccharides: Every baby needs a sugar mama. Glycobiology. 2012; 22: 1147-1162. doi: 10.1093/glycob/cws074 PMID: 22513036
    • (2012) Glycobiology. , vol.22 , pp. 1147-1162
    • Bode, L.1
  • 4
    • 84871967105 scopus 로고    scopus 로고
    • The principal fucosylated oligosaccharides of human milk exhibit prebiotic properties on cultured infant microbiota
    • 23028202
    • Yu ZT, Chen C, Kling DE, Liu B, McCoy JM, Merighi M, et al. The principal fucosylated oligosaccharides of human milk exhibit prebiotic properties on cultured infant microbiota. Glycobiology. 2013; 23: 169-177. doi: 10.1093/glycob/cws138 PMID: 23028202
    • (2013) Glycobiology. , vol.23 , pp. 169-177
    • Yu, Z.T.1    Chen, C.2    Kling, D.E.3    Liu, B.4    McCoy, J.M.5    Merighi, M.6
  • 5
  • 6
    • 0013238319 scopus 로고    scopus 로고
    • Campylobacter jejuni binds intestinal H(O) antigen (Fuc alpha 1, 2Gal beta 1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection
    • 12562767
    • Ruiz-Palacios GM, Cervantes LE, Ramos P, Chavez-Munguia B, Newburg DS. Campylobacter jejuni binds intestinal H(O) antigen (Fuc alpha 1, 2Gal beta 1, 4GlcNAc), and fucosyloligosaccharides of human milk inhibit its binding and infection. J Biol Chem. 2003; 278: 14112-14120. PMID: 12562767
    • (2003) J Biol Chem. , vol.278 , pp. 14112-14120
    • Ruiz-Palacios, G.M.1    Cervantes, L.E.2    Ramos, P.3    Chavez-Munguia, B.4    Newburg, D.S.5
  • 7
    • 84884834681 scopus 로고    scopus 로고
    • Fucosylated but not sialylated milk oligosaccharides diminish colon motor contractions
    • 24098451
    • Bienenstock J, Buck RH, Linke H, Forsythe P, Stanisz AM, Kunze WA. Fucosylated but not sialylated milk oligosaccharides diminish colon motor contractions. PloS One. 2013; 8: e76236. doi: 10.1371/ journal.pone.0076236 PMID: 24098451
    • (2013) PloS One. , vol.8
    • Bienenstock, J.1    Buck, R.H.2    Linke, H.3    Forsythe, P.4    Stanisz, A.M.5    Kunze, W.A.6
  • 8
    • 84907930217 scopus 로고    scopus 로고
    • Methods for improving enzymatic trans-glycosylation for synthesis of human milk oligosaccharide biomimetics
    • 25208138
    • Zeuner B, Jers C, Mikkelsen JD, Meyer AS. Methods for improving enzymatic trans-glycosylation for synthesis of human milk oligosaccharide biomimetics. J Agric Food Chem. 2014; 62: 9615-9631. doi: 10.1021/jf502619p PMID: 25208138
    • (2014) J Agric Food Chem. , vol.62 , pp. 9615-9631
    • Zeuner, B.1    Jers, C.2    Mikkelsen, J.D.3    Meyer, A.S.4
  • 9
    • 0026055308 scopus 로고
    • A classification of glycosyl hydrolases based on amino acid sequence similarities
    • 1747104
    • Henrissat B. A classification of glycosyl hydrolases based on amino acid sequence similarities. Biochem J. 1991; 280: 309-316. PMID: 1747104
    • (1991) Biochem J. , vol.280 , pp. 309-316
    • Henrissat, B.1
  • 10
    • 0042527531 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of the family 29 α-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant
    • 12911294
    • Cobucci-Ponzano B, Trincone A, Giordano A, Rossi M, Moracci M. Identification of the catalytic nucleophile of the family 29 α-L-fucosidase from Sulfolobus solfataricus via chemical rescue of an inactive mutant. Biochemistry. 2003; 42: 9525-9531. PMID: 12911294
    • (2003) Biochemistry. , vol.42 , pp. 9525-9531
    • Cobucci-Ponzano, B.1    Trincone, A.2    Giordano, A.3    Rossi, M.4    Moracci, M.5
  • 11
    • 0346220296 scopus 로고    scopus 로고
    • Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosyl-enzyme intermediate and mutagenesis
    • 12975375
    • Tarling CA, He S, Sulzenbacher G, Bignon C, Bourne Y, Henrissat B, et al. Identification of the catalytic nucleophile of the family 29 alpha-L-fucosidase from Thermotoga maritima through trapping of a covalent glycosyl-enzyme intermediate and mutagenesis. J Biol Chem. 2003; 278: 47394-47399. PMID: 12975375
    • (2003) J Biol Chem. , vol.278 , pp. 47394-47399
    • Tarling, C.A.1    He, S.2    Sulzenbacher, G.3    Bignon, C.4    Bourne, Y.5    Henrissat, B.6
  • 12
    • 0032832941 scopus 로고    scopus 로고
    • Enzymatic synthesis of alpha-L-fucosyl-N-acetyllactosamines and 3'-O-alpha-L-fucosyllactose utilizing alpha-L-fucosidases
    • 10573857
    • Murata T, Morimoto S, Zeng X, Watanabe S, Usui T. Enzymatic synthesis of alpha-L-fucosyl-N-acetyllactosamines and 3'-O-alpha-L-fucosyllactose utilizing alpha-L-fucosidases. Carbohydr Res. 1999; 320: 192-199. PMID: 10573857
    • (1999) Carbohydr Res. , vol.320 , pp. 192-199
    • Murata, T.1    Morimoto, S.2    Zeng, X.3    Watanabe, S.4    Usui, T.5
  • 13
    • 84867731329 scopus 로고    scopus 로고
    • Biotechnological production of human milk oligosaccharides
    • 22119239
    • Han NS, Kim TJ, Park YC, Kim J, Seo JH. Biotechnological production of human milk oligosaccharides. Biotechnol Adv. 2012; 30: 1268-1278. doi: 10.1016/j.biotechadv.2011.11.003 PMID: 22119239
    • (2012) Biotechnol Adv. , vol.30 , pp. 1268-1278
    • Han, N.S.1    Kim, T.J.2    Park, Y.C.3    Kim, J.4    Seo, J.H.5
  • 14
    • 0035787060 scopus 로고    scopus 로고
    • Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells
    • 11762172
    • Pauly M, Eberhard S, Albersheim P, Darvill A, York WS. Effects of the mur1 mutation on xyloglucans produced by suspension-cultured Arabidopsis thaliana cells. Planta. 2001; 214: 67-74. PMID: 11762172
    • (2001) Planta. , vol.214 , pp. 67-74
    • Pauly, M.1    Eberhard, S.2    Albersheim, P.3    Darvill, A.4    York, W.S.5
  • 15
    • 33846591870 scopus 로고    scopus 로고
    • Directed evolution of the α-L-fucosidase from Thermotoga maritima into an α-L-transfucosidase
    • 17240986
    • Osanjo G, Dion M, Drone J, Solleux C, Tran V, Rabiller C, et al. Directed evolution of the α-L-fucosidase from Thermotoga maritima into an α-L-transfucosidase. Biochemistry. 2007; 46: 1022-1033. PMID: 17240986
    • (2007) Biochemistry. , vol.46 , pp. 1022-1033
    • Osanjo, G.1    Dion, M.2    Drone, J.3    Solleux, C.4    Tran, V.5    Rabiller, C.6
  • 16
    • 1842477147 scopus 로고    scopus 로고
    • Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis
    • 14715651
    • Sulzenbacher G, Bignon C, Nishimura T, Tarling CA, Withers SG, Henrissat B, et al. Crystal structure of Thermotoga maritima alpha-L-fucosidase. Insights into the catalytic mechanism and the molecular basis for fucosidosis. J Biol Chem. 2004; 279: 13119-13128. PMID: 14715651
    • (2004) J Biol Chem. , vol.279 , pp. 13119-13128
    • Sulzenbacher, G.1    Bignon, C.2    Nishimura, T.3    Tarling, C.A.4    Withers, S.G.5    Henrissat, B.6
  • 17
    • 79953210780 scopus 로고    scopus 로고
    • Metagenomic analyses: Past and future trends
    • 21169428
    • Simon C, Daniel R. Metagenomic analyses: Past and future trends. Appl Environ Microbiol. 2011; 77: 1153-1161. doi: 10.1128/AEM.02345-10 PMID: 21169428
    • (2011) Appl Environ Microbiol. , vol.77 , pp. 1153-1161
    • Simon, C.1    Daniel, R.2
  • 18
    • 73849152593 scopus 로고    scopus 로고
    • Metagenomic gene discovery: How far have we moved into novel sequence space?
    • 19946882
    • Tuffin M, Anderson D, Heath C, Cowan DA. Metagenomic gene discovery: how far have we moved into novel sequence space? Biotechnol J. 2009; 4: 1671-1683. doi: 10.1002/biot.200900235 PMID: 19946882
    • (2009) Biotechnol J. , vol.4 , pp. 1671-1683
    • Tuffin, M.1    Anderson, D.2    Heath, C.3    Cowan, D.A.4
  • 19
    • 84903759424 scopus 로고    scopus 로고
    • Bioprospecting potential of the soil metagenome: Novel enzymes and bioactivities
    • 24124406
    • Lee MH, Lee SW. Bioprospecting potential of the soil metagenome: novel enzymes and bioactivities. Genomics Inform. 2013; 11: 114-120. doi: 10.5808/GI.2013.11.3.114 PMID: 24124406
    • (2013) Genomics Inform. , vol.11 , pp. 114-120
    • Lee, M.H.1    Lee, S.W.2
  • 20
    • 84873619196 scopus 로고    scopus 로고
    • Enzymatic depolymerization of gum tragacanth: Bifidogenic potential of low molecular weight oligosaccharides
    • 23343141
    • Gavlighi HA, Michalak M, Meyer AS, Mikkelsen JD. Enzymatic depolymerization of gum tragacanth: bifidogenic potential of low molecular weight oligosaccharides. J Agric Food Chem. 2013; 61: 1272-1278. doi: 10.1021/jf304795f PMID: 23343141
    • (2013) J Agric Food Chem. , vol.61 , pp. 1272-1278
    • Gavlighi, H.A.1    Michalak, M.2    Meyer, A.S.3    Mikkelsen, J.D.4
  • 21
    • 84871396799 scopus 로고    scopus 로고
    • Ray Meta: Scalable de novo metagenome assembly and profiling
    • 23259615
    • Boisvert S, Raymond F, Godzaridis É, Laviolette F, Corbeil J. Ray Meta: Scalable de novo metagenome assembly and profiling. Genome Biol. 2012; 13: R122. doi: 10.1186/gb-2012-13-12-r122 PMID: 23259615
    • (2012) Genome Biol. , vol.13 , pp. R122
    • Boisvert, S.1    Raymond, F.2    Godzaridis, É.3    Laviolette, F.4    Corbeil, J.5
  • 22
  • 24
    • 34250207393 scopus 로고    scopus 로고
    • High-throughput mapping of cell-wall polymers within and between plants using novel microarrays
    • 17565618
    • Moller I, Sørensen I, Bernal AJ, Blaukopf C, Lee K, Øbro J, et al. High-throughput mapping of cell-wall polymers within and between plants using novel microarrays. Plant J. 2007; 50: 1118-1128. PMID: 17565618
    • (2007) Plant J. , vol.50 , pp. 1118-1128
    • Moller, I.1    Sørensen, I.2    Bernal, A.J.3    Blaukopf, C.4    Lee, K.5    Øbro, J.6
  • 25
    • 0026940759 scopus 로고
    • NMR spectroscopy in the structural elucidation of oligosaccharides and glycosides
    • 1368855
    • Agrawal PK. NMR spectroscopy in the structural elucidation of oligosaccharides and glycosides. Phytochemistry. 1992; 31: 3307-3330. PMID: 1368855
    • (1992) Phytochemistry. , vol.31 , pp. 3307-3330
    • Agrawal, P.K.1
  • 26
    • 0034508404 scopus 로고    scopus 로고
    • Carbohydrate structural determination by NMR spectroscopy: Modern methods and limitations
    • 11749359
    • Duus JØ, Gotfredsen CH, Bock K. Carbohydrate structural determination by NMR spectroscopy: Modern methods and limitations. Chem Rev. 2000; 100: 4589-4614. PMID: 11749359
    • (2000) Chem Rev. , vol.100 , pp. 4589-4614
    • Duus, J.Ø.1    Gotfredsen, C.H.2    Bock, K.3
  • 27
    • 84880939975 scopus 로고    scopus 로고
    • α-L-fucosidase from Paenibacillus thiaminolyticus: Its hydrolytic and transglycosylation abilities
    • 23723440
    • Benesová E, Lipovová P, Dvoráková H, Králová B. α-L-fucosidase from Paenibacillus thiaminolyticus: its hydrolytic and transglycosylation abilities. Glycobiology. 2013; 23: 1052-1065. doi: 10.1093/glycob/ cwt041 PMID: 23723440
    • (2013) Glycobiology. , vol.23 , pp. 1052-1065
    • Benesová, E.1    Lipovová, P.2    Dvoráková, H.3    Králová, B.4
  • 29
    • 78149297086 scopus 로고    scopus 로고
    • CAZymes analysis toolkit (CAT): Web service for searching and analyzing carbohydrate-active enzymes in a newly sequenced organism using CAZy database
    • 20696711
    • Park BH, Karpinets TV, Syed MH, Leuze MR, Uberbacher EC. CAZymes analysis toolkit (CAT): Web service for searching and analyzing carbohydrate-active enzymes in a newly sequenced organism using CAZy database. Glycobiology. 2010; 20: 1574-1584. doi: 10.1093/glycob/cwq106 PMID: 20696711
    • (2010) Glycobiology. , vol.20 , pp. 1574-1584
    • Park, B.H.1    Karpinets, T.V.2    Syed, M.H.3    Leuze, M.R.4    Uberbacher, E.C.5
  • 30
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • 3447015
    • Saitou N, Nei M. The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol Biol Evol. 1987; 4: 406-425. PMID: 3447015
    • (1987) Mol Biol Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 31
    • 84890330527 scopus 로고    scopus 로고
    • MEGA6: Molecular Evolutionary Genetics Analysis version 6.0
    • 24132122
    • Tamura K, Stecher G, Peterson D, Filipski A, Kumar S. MEGA6: Molecular Evolutionary Genetics Analysis version 6.0. Mol Biol Evol. 2013; 30: 2725-2729. doi: 10.1093/molbev/mst197 PMID: 24132122
    • (2013) Mol Biol Evol. , vol.30 , pp. 2725-2729
    • Tamura, K.1    Stecher, G.2    Peterson, D.3    Filipski, A.4    Kumar, S.5
  • 32
    • 84969426536 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J. Confidence Limits on Phylogenies: An Approach Using the Bootstrap. Evolution. 1985; 39: 783-791.
    • (1985) Evolution. , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 33
    • 84861439238 scopus 로고    scopus 로고
    • Differences in the substrate specificities and active-site structures of two α-L-fucosidases (glycoside hydrolase family 29) from Bacteroides thetaiotaomicron
    • 22738979
    • Sakurama H, Tsutsumi E, Ashida H, Katayama T, Yamamoto K, Kumagai H. Differences in the substrate specificities and active-site structures of two α-L-fucosidases (glycoside hydrolase family 29) from Bacteroides thetaiotaomicron. Biosci Biotechnol Biochem. 2012; 76: 1022-1024. PMID: 22738979
    • (2012) Biosci Biotechnol Biochem. , vol.76 , pp. 1022-1024
    • Sakurama, H.1    Tsutsumi, E.2    Ashida, H.3    Katayama, T.4    Yamamoto, K.5    Kumagai, H.6
  • 34
    • 84895069393 scopus 로고    scopus 로고
    • Biocatalytic production of 3'-sialyllactose by use of a modified sialidase with superior trans-sialidase activity
    • Michalak M, Larsen DM, Jers C, Almeida JR, Willer M, Li H, et al. Biocatalytic production of 3'-sialyllactose by use of a modified sialidase with superior trans-sialidase activity. Process Biochem. 2014; 49: 265-270.
    • (2014) Process Biochem. , vol.49 , pp. 265-270
    • Michalak, M.1    Larsen, D.M.2    Jers, C.3    Almeida, J.R.4    Willer, M.5    Li, H.6
  • 35
    • 84907164436 scopus 로고    scopus 로고
    • Structure and substrate specificity of a eukaryotic fucosidase from Fusarium graminearum
    • 25086049
    • Cao H, Walton JD, Brumm P, Phillips GN Jr. Structure and substrate specificity of a eukaryotic fucosidase from Fusarium graminearum. J Biol Chem. 2014; 289: 25624-25638. doi: 10.1074/jbc.M114. 583286 PMID: 25086049
    • (2014) J Biol Chem. , vol.289 , pp. 25624-25638
    • Cao, H.1    Walton, J.D.2    Brumm, P.3    Phillips, G.N.4
  • 36
    • 0005958575 scopus 로고    scopus 로고
    • Enzyme data and metabolic information: BRENDA, a resource for research in biology, biochemistry, and medicine
    • Schomburg I, Hofmann O, Baensch C, Chang A, Schomburg D. Enzyme data and metabolic information: BRENDA, a resource for research in biology, biochemistry, and medicine. Gene Function & Disease. 2000; 1: 109-118.
    • (2000) Gene Function & Disease. , vol.1 , pp. 109-118
    • Schomburg, I.1    Hofmann, O.2    Baensch, C.3    Chang, A.4    Schomburg, D.5
  • 37
    • 38849107515 scopus 로고    scopus 로고
    • A Novel α1,2-L-fucosidase acting on xyloglucan oligosaccharides is associated with endo-beta-mannosidase
    • 17956906
    • Ishimizu T, Hashimoto C, Takeda R, Fujii K, Hase S. A Novel α1,2-L-fucosidase acting on xyloglucan oligosaccharides is associated with endo-beta-mannosidase. J Biochem. 2007; 142: 721-729. PMID: 17956906
    • (2007) J Biochem. , vol.142 , pp. 721-729
    • Ishimizu, T.1    Hashimoto, C.2    Takeda, R.3    Fujii, K.4    Hase, S.5
  • 38
    • 84878566892 scopus 로고    scopus 로고
    • Synthesis of fucosyl-N-acetylglucosamine disaccharides by transfucosylation using α-L-fucosidases from Lactobacillus casei
    • 23542622
    • Rodríguez-Díaz J, Carbajo RJ, Pineda-Lucena A, Monedero V, Yebra MJ. Synthesis of fucosyl-N-acetylglucosamine disaccharides by transfucosylation using α-L-fucosidases from Lactobacillus casei. Appl Environ Microbiol. 2013; 79: 3847-3850. doi: 10.1128/AEM.00229-13 PMID: 23542622
    • (2013) Appl Environ Microbiol. , vol.79 , pp. 3847-3850
    • Rodríguez-Díaz, J.1    Carbajo, R.J.2    Pineda-Lucena, A.3    Monedero, V.4    Yebra, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.